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Literature summary extracted from

  • Neehaul, Y.; Juarez, O.; Barquera, B.; Hellwig, P.
    Infrared spectroscopic evidence of a redox-dependent conformational change involving ion binding residue NqrB-D397 in the Na+-pumping NADH quinone oxidoreductase from Vibrio cholerae (2013), Biochemistry, 52, 3085-3093 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
7.2.1.1 D397E subunit NqrB. In the mutant, the spectral features characteristic of COOH groups are shifted, and the hydrogen binding of the ion binding cluster is weakened Vibrio cholerae serotype O1

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.1.1 Rb+ presence of Rb+ induces conformational changes, indicating a changed accessibility of the sodium binding sites Vibrio cholerae serotype O1

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.1 K+ Na+-NQR undergoes significant conformational changes upon oxidoreduction, depending on the monovalent cation present (Na+, Li+, K+, or Rb+). Deprotonated acid residues are involved in the binding of cations, pointing toward a monodentate binding mode in the oxidized form of the enzyme and bidentate binding in the reduced form Vibrio cholerae serotype O1
7.2.1.1 Li+ Na+-NQR undergoes significant conformational changes upon oxidoreduction, depending on the monovalent cation present (Na+, Li+, K+, or Rb+). Deprotonated acid residues are involved in the binding of cations, pointing toward a monodentate binding mode in the oxidized form of the enzyme and bidentate binding in the reduced form. Residue D397 is one of the acid residues involved in Na+ and Li+ binding Vibrio cholerae serotype O1
7.2.1.1 Na+ Na+-NQR undergoes significant conformational changes upon oxidoreduction, depending on the monovalent cation present (Na+, Li+, K+, or Rb+). Deprotonated acid residues are involved in the binding of cations, pointing toward a monodentate binding mode in the oxidized form of the enzyme and bidentate binding in the reduced form. Residue D397 is one of the acid residues involved in Na+ and Li+ binding Vibrio cholerae serotype O1

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Vibrio cholerae serotype O1 A5F5X1 and A5F5X0 and A5F5Y7 and A5F5Y6 and A5F5Y3 and A5F5Y4 A5F5X1: subunit NqrA, A5F5X0: subunit NqrB, A5F5Y7: subunit NqrC, A5F5Y6: subunit NqrD; A5F5Y3: subunit NqrE, A5F5Y4: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon.
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7.2.1.1 Vibrio cholerae serotype O1 ATCC 39541 A5F5X1 and A5F5X0 and A5F5Y7 and A5F5Y6 and A5F5Y3 and A5F5Y4 A5F5X1: subunit NqrA, A5F5X0: subunit NqrB, A5F5Y7: subunit NqrC, A5F5Y6: subunit NqrD; A5F5Y3: subunit NqrE, A5F5Y4: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon.
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Synonyms

EC Number Synonyms Comment Organism
7.2.1.1 Na(+)-translocating NADH-quinone reductase subunit B
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 Vibrio cholerae serotype O1
7.2.1.1 NqrB
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 Vibrio cholerae serotype O1